Structure of PDB 4c3o Chain D

Receptor sequence
>4c3oD (length=262) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2) [Search protein sequence]
PRTPVIWLHGLECTCCTESFIRSAHPLAKDAILSLISLDYDDTIMAAAGQ
QAEQALADVMREYKGNYIVAVEGNAPLNEDGMFCILAGEPFLEKLKRVSA
DAKAIIAWGSCASWGCVQAARPNPTKATPVHKLITDKPIIKVPGCPPIPE
VMSAVITYMLAFDRIPPLDRLGRPKMFYGQRIHDKCYRRAHFDAGQFVEA
WDDEGARKGYCLYKMGCKGPTTYNACSTVRWNDGVSFPIQSGHGCLGCSE
DGFWDYGSFYSR
3D structure
PDB4c3o How the Structure of the Large Subunit Controls Function in an Oxygen-Tolerant [Nife]-Hydrogenase.
ChainD
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C17 C20 C115 C149 H187 C190 C215 C221 C230 P242 C249 C252
Catalytic site (residue number reindexed from 1) C13 C16 C111 C145 H183 C186 C211 C217 C226 P238 C245 C248
Enzyme Commision number 1.12.99.6: hydrogenase (acceptor).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SF4 D H187 C190 R192 R193 C215 L216 Y217 C221 I243 H183 C186 R188 R189 C211 L212 Y213 C217 I239
BS02 F3S D I186 N228 C230 W235 P242 C249 L250 C252 I182 N224 C226 W231 P238 C245 L246 C248
BS03 F4S D E16 C17 C19 C20 E76 C115 C120 C149 E12 C13 C15 C16 E72 C111 C116 C145
Gene Ontology
Molecular Function
GO:0008901 ferredoxin hydrogenase activity
GO:0051536 iron-sulfur cluster binding
Cellular Component
GO:0009375 ferredoxin hydrogenase complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:4c3o, PDBe:4c3o, PDBj:4c3o
PDBsum4c3o
PubMed24428762
UniProtQ8ZPG9

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